Examining the role of hydrogen bonding interactions in the substrate specificity for the loading step of polyketide synthase thioesterase domains.
about
Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates.Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?A thioesterase from an iterative fungal polyketide synthase shows macrocyclization and cross coupling activity and may play a role in controlling iterative cycling through product offloading.A Single Active Site Mutation in the Pikromycin Thioesterase Generates a More Effective Macrocyclization Catalyst.Biosynthesis of ebelactone A: isotopic tracer, advanced precursor and genetic studies reveal a thioesterase-independent cyclization to give a polyketide β-lactone.
P2860
Examining the role of hydrogen bonding interactions in the substrate specificity for the loading step of polyketide synthase thioesterase domains.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年學術文章
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name
Examining the role of hydrogen ...... synthase thioesterase domains.
@en
Examining the role of hydrogen ...... synthase thioesterase domains.
@nl
type
label
Examining the role of hydrogen ...... synthase thioesterase domains.
@en
Examining the role of hydrogen ...... synthase thioesterase domains.
@nl
prefLabel
Examining the role of hydrogen ...... synthase thioesterase domains.
@en
Examining the role of hydrogen ...... synthase thioesterase domains.
@nl
P356
P1433
P1476
Examining the role of hydrogen ...... synthase thioesterase domains.
@en
P2093
P304
11793-11803
P356
10.1021/BI800963Y
P407
P577
2008-10-14T00:00:00Z